期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
卷 1543, 期 2, 页码 239-252出版社
ELSEVIER
DOI: 10.1016/S0167-4838(00)00247-8
关键词
cellulase; endoglucanase; cellobiohydrolase; protein engineering; site-directed mutagenesis; structure; oligosaccharide synthesis
Cellulases are enzymes which hydrolyse the beta -1,4-glucosidic linkages of cellulose. They fall into 13 of the 82 glycoside hydrolase families identified by sequence analysis, but they are traditionally divided into two classes termed 'endoglucanases' (EC 3.2.1.4) and 'cellobiohydrolases' (3.2.1.91). Both types of cellulases degrade soluble cellodextrins and amorphous cellulose but, with a few notable exceptions, it is only the cellobiohydrolases which degrade crystalline cellulose efficiently. Site-directed mutagenesis has been central to the characterisation of cellulases, ranging from the identification and characterisation of putative catalytic and binding residues, the trapping of enzyme-substrate complexes by crystallography through to the construction of new and improved biocatalysts including 'glycosynthases'. Whilst studies on soluble substrates and substrate analogues have provided a wealth of information, understanding the mechanism of degradation of the natural substrate, crystalline cellulose, remains a great challenge. (C) 2000 Elsevier Science B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据